TY - JOUR
T1 - Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans
AU - Lye, R. J.
AU - Porter, M. E.
AU - Scholey, J. M.
AU - McIntosh, J. R.
PY - 1987/10/23
Y1 - 1987/10/23
N2 - C. elegans contains a microtubule binding protein that resembles both dynein and kinesin. This protein has a MgATPase activity and copurifies on both sucrose gradients and DEAE Sephadex columns with a polypeptide of Mr approximately 400 kd. The ATPase activity is 50% inhibited by 10 μM vanadate, 1 mM N-ethyl maleimide, or 5 mM AMP-PNP; it is enhanced 50% by 0.2% Triton. The 400 kd polypeptide is cleaved at a single site by ultraviolet light in the presence of ATP and vanadate. In these ways, the protein resembles dynein. The protein also promotes ATP-dependent translocation of microtubules or axonemes, "plus" ends trailing. This property is kinesin-like; however, the motility is blocked by 5 μM vanadate, 1 mM N-ethyl maleimide, 0.5 mM ATP-γ-S, or by ATP-vanadate-UV cleavage of the 400 kd polypeptide, characteristics that differ from kinesin. We propose that this protein is a novel microtubule translocator.
AB - C. elegans contains a microtubule binding protein that resembles both dynein and kinesin. This protein has a MgATPase activity and copurifies on both sucrose gradients and DEAE Sephadex columns with a polypeptide of Mr approximately 400 kd. The ATPase activity is 50% inhibited by 10 μM vanadate, 1 mM N-ethyl maleimide, or 5 mM AMP-PNP; it is enhanced 50% by 0.2% Triton. The 400 kd polypeptide is cleaved at a single site by ultraviolet light in the presence of ATP and vanadate. In these ways, the protein resembles dynein. The protein also promotes ATP-dependent translocation of microtubules or axonemes, "plus" ends trailing. This property is kinesin-like; however, the motility is blocked by 5 μM vanadate, 1 mM N-ethyl maleimide, 0.5 mM ATP-γ-S, or by ATP-vanadate-UV cleavage of the 400 kd polypeptide, characteristics that differ from kinesin. We propose that this protein is a novel microtubule translocator.
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U2 - 10.1016/0092-8674(87)90157-7
DO - 10.1016/0092-8674(87)90157-7
M3 - Article
C2 - 2959372
AN - SCOPUS:0023663075
VL - 51
SP - 309
EP - 318
JO - Cell
JF - Cell
SN - 0092-8674
IS - 2
ER -